[HTML][HTML] Distinct glycan structures of uroplakins Ia and Ib: structural basis for the selective binding of FimH adhesin to uroplakin Ia
B Xie, G Zhou, SY Chan, E Shapiro, XP Kong… - Journal of Biological …, 2006 - ASBMB
Although it has been shown that mouse uroplakin (UP) Ia, a major glycoprotein of urothelial
apical surface, can serve as the receptor for the FimH lectin adhesin of type 1-fimbriated
Escherichia coli, the organism that causes a great majority of urinary tract infections, the
glycan structure of this native receptor was unknown. Using a sensitive approach that
combines in-gel glycosidase and protease digestions, permethylation of released glycans,
and mass spectrometry, we have elucidated for the first time the native glycoform structures …
apical surface, can serve as the receptor for the FimH lectin adhesin of type 1-fimbriated
Escherichia coli, the organism that causes a great majority of urinary tract infections, the
glycan structure of this native receptor was unknown. Using a sensitive approach that
combines in-gel glycosidase and protease digestions, permethylation of released glycans,
and mass spectrometry, we have elucidated for the first time the native glycoform structures …